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Difference between revisions of "User:Beatrice Cobucci-Ponzano"
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She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases. | She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases ([[GH29]]) <cite>PMID12569098 PMID12911294 PMID15835922</cite>, and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases <cite>PMID19875083</cite>. This method could be of general applicability to all alpha-glycosidases. | ||
| − | Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the | + | Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family [[GH116]] <cite>PMID20427274</cite>. |
Revision as of 06:16, 14 June 2010
Beatrice Cobucci-Ponzano obtained her degree in Biology from the University of Naples “Federico II”, Italy, in 1997, working on the beta-glycosidase (GH1) from the archaeon Sulfolobus solfataricus, under the supervision of Mosè Rossi at the Institute of Protein Biochemistry (IBP) of the italian National Research Council (CNR).
She obtained her PhD in Biochemistry and Biophysic at the University of Padua, working on the characterization of CAZymes form hyperthermophiles (GH1 and GH31) under the supervision of Marco Moracci at IBP.
From 2001 she is staff scientist at IBP in the group of Marco Moracci. The work focuses on the characterization and the understanding of the reaction mechanism of glycoside hydrolases, on their modification for the synthesis of glycosides (glycosynthases), and on glycosyltransferases.
She has determined the reaction mechanism and the catalytic residues of alpha-L-fucosidases (GH29) [1, 2, 3], and developed a new method for the modification of this class of enzymes in efficient alpha-L-fucosynthases [4]. This method could be of general applicability to all alpha-glycosidases.
Recently, she characterized a novel archaeal beta-glycosidase that allowed the creation of the CAZy family GH116 [5].
Reference list
- Cobucci-Ponzano B, Trincone A, Giordano A, Rossi M, and Moracci M. (2003). Identification of an archaeal alpha-L-fucosidase encoded by an interrupted gene. Production of a functional enzyme by mutations mimicking programmed -1 frameshifting. J Biol Chem. 2003;278(17):14622-31. DOI:10.1074/jbc.M211834200 |
- Cobucci-Ponzano B, Trincone A, Giordano A, Rossi M, and Moracci M. (2003). Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry. 2003;42(32):9525-31. DOI:10.1021/bi035036t |
- Cobucci-Ponzano B, Mazzone M, Rossi M, and Moracci M. (2005). Probing the catalytically essential residues of the alpha-L-fucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. Biochemistry. 2005;44(16):6331-42. DOI:10.1021/bi047495f |
- Cobucci-Ponzano B, Conte F, Bedini E, Corsaro MM, Parrilli M, Sulzenbacher G, Lipski A, Dal Piaz F, Lepore L, Rossi M, and Moracci M. (2009). beta-Glycosyl azides as substrates for alpha-glycosynthases: preparation of efficient alpha-L-fucosynthases. Chem Biol. 2009;16(10):1097-108. DOI:10.1016/j.chembiol.2009.09.013 |
- Cobucci-Ponzano B, Aurilia V, Riccio G, Henrissat B, Coutinho PM, Strazzulli A, Padula A, Corsaro MM, Pieretti G, Pocsfalvi G, Fiume I, Cannio R, Rossi M, and Moracci M. (2010). A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2. J Biol Chem. 2010;285(27):20691-703. DOI:10.1074/jbc.M109.086470 |